ID G1R6R5_NOMLE Unreviewed; 1696 AA.
AC G1R6R5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Tensin 1 {ECO:0000313|Ensembl:ENSNLEP00000008887.2};
GN Name=TNS1 {ECO:0000313|Ensembl:ENSNLEP00000008887.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000008887.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000008887.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000008887.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000256|ARBA:ARBA00007881}.
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DR EMBL; ADFV01110712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01110713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01110714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01110715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01110716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01110717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01110718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01110719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 61853.ENSNLEP00000008887; -.
DR Ensembl; ENSNLET00000009307.2; ENSNLEP00000008887.2; ENSNLEG00000007284.3.
DR eggNOG; KOG1930; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR GeneTree; ENSGT00940000155400; -.
DR HOGENOM; CLU_002189_2_0_1; -.
DR InParanoid; G1R6R5; -.
DR OMA; RYKQADN; -.
DR TreeFam; TF315996; -.
DR Proteomes; UP000001073; Chromosome 22a.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0007044; P:cell-substrate junction assembly; IEA:Ensembl.
DR GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd14560; PTP_tensin-1; 1.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR013625; PTB.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR033929; Tensin_PTB.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR PANTHER; PTHR45734; TENSIN; 1.
DR PANTHER; PTHR45734:SF3; TENSIN-1; 1.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50001; SH2; 1.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 4..176
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 169..297
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1432..1533
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 367..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1333..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..822
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1696 AA; 181870 MW; AF951B6DA6E75717 CRC64;
MSVSRTMEDS CELDLVYVTE RIIAVSFPST ANEENFRSNL REVAQMLKSK HGGNYLLFNL
SERRPDITKL HAKVLEFGWP DLHTPALEKI CSICKAMDTW LNADPHNVVV LHNKGNRGRI
GVVIAAYMHY SNISASADQA LDRFAMKRFY EDKIVPVGQP SQRRYVHYFS GLLSGSIKMN
NKPLFLHHVI MRCRPFLRIY QAMQPVYTSG IYNIPGDSQT SVCITIEPGL LLKGDILLKC
YHKKFRSPAR DVIFRVQFHT CAIHDLGVVF GKEDLDDAFK DDRFPEYGKV EFVFSYGPEK
IQGMEHLENG PSVSVDYNTS DPLIRWDSYD NFSGHRDDGM EEVVGHTQGP LDGSLYAKVK
KKDSLHGSTG AVNATRPTLS ATPNHVEHTL SVSSDSGNST ASTKTDKTDE PVPGASSATA
ALSPQEKREL DRLLSGFGLE REKQGAMYHT QHLRSRPAGG LAVPSSGRHV VPAQVHVNGG
ALASERETDI LDDELPNQDG HSAGSMGTLS SLDGVTNTSE GGYPEALSPL TNGLDKPYPM
EPMVNGGGYP YESASRAGPA HAGHTAPMRP SYSAQEGLAG YQREGPHPAW PQPVTTAHYA
HDPSGMFRSQ SFFDQLPPAP VFYTVQRGMN SCQQQQQQQQ QQPRPPPRRQ ERVHQESLVA
SRPSPQPLAE TPIPSLPEFP RAASQQEIEQ SIETLNMLML DLEPASTAAP LHKSQSVPGA
WPGASPLSSQ PLSGSSRQSH PLTQSRSGYI PTGHSLGTPE PAPRASLESV PPGRSYSPYD
YQPCLAGPNQ DFHSKSPASS SLPAFLPTTH SPPGPQQPPA SLPGLTAQPL LSPKEATSDP
SRTPEEEPLN LEGLVAHRVA GVQAREKQPA EPPAPLRRRA ASDGQYENQS PEATSPRSPG
VRSPVQCVSP ELALTIALNP GGRPKEPHLH SYKEAFEEME GTSPSSPPPS GVRSPPGLAK
TPLSALGLKP HNPADILLHP TGEEDEGKVV VRLSEEPRSY VESVARTAVA GPRAQDSEPK
SFSAPATQAY GHEIPLRNGT LGGSFVSPSP LSTSSPILSA DSTSVGSFPS GESSDQGPRT
PTQPLLESGF RSGSLGQPSP SAQRNYQSSS PLPTVGSSYS SPDYSLQQFS SSPESQARAQ
FSVAGIHTVP GSPQARHRTV GTNTLPSPGF GRRAINPSMA APGSPSMSHR QMMGPPGTGF
HGSTVSSPQS SAATTPGSPS LGRHPAGAYQ VSGLHTMCTP RGVPAWAGIW GSQGNLASGL
HSNAIASPGS RHLGGSGSVV PGSPCLDRHV AYGGYSTPED RRPTLSRQSS ASGYQAPSTP
SFPVCPAYYP GLSSPATSPS PDSAAFRQGS PTPALPEKRR MSVGDRAGSL PNYATINGKV
SSPVASGMSS PSGGSTVSFS HTLPDFSKYS MPDNSPETRA KVKFVQDTSK YWYKPEISRE
QAIALLKDQE PGAFIIRDSH SFRGAYGLAM KVSSPPPTIV QQNKKGDMTH ELVRHFLIET
GPRGVKLKGS LSALVYQHSI IPLALPCKLV IPNRDPTDES KDSSGPANST ADLLKQGAAC
NVLFVNSVDM ESLTGPQAIS KATSETLAAD PTPAATIVHF KVSAQGITLT DNQRKLFFRR
HYPLNTVTFC DLDPQERKWM KTEGGAPAKL FGFVARKQGS TTDNACHLFA ELDPNQPASA
IVNFVSKVML NAGQKR
//
